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| | ==Crystal structure of TioX from Micromonospora sp. ML1== | | ==Crystal structure of TioX from Micromonospora sp. ML1== |
| - | <StructureSection load='3itw' size='340' side='right' caption='[[3itw]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3itw' size='340' side='right'caption='[[3itw]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3itw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Micromonospora_sp._ml1 Micromonospora sp. ml1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ITW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ITW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3itw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_sp._ML1 Micromonospora sp. ML1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ITW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ITW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tioX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=349725 Micromonospora sp. ML1])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3itw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3itw OCA], [http://pdbe.org/3itw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3itw RCSB], [http://www.ebi.ac.uk/pdbsum/3itw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3itw ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3itw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3itw OCA], [https://pdbe.org/3itw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3itw RCSB], [https://www.ebi.ac.uk/pdbsum/3itw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3itw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/it/3itw_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/it/3itw_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micromonospora sp. ml1]] | + | [[Category: Large Structures]] |
| - | [[Category: Biswas, T]] | + | [[Category: Micromonospora sp. ML1]] |
| - | [[Category: Garneau-Tsodikova, S]] | + | [[Category: Biswas T]] |
| - | [[Category: Tsodikov, O V]] | + | [[Category: Garneau-Tsodikova S]] |
| - | [[Category: Bisintercalator]]
| + | [[Category: Tsodikov OV]] |
| - | [[Category: Bleomycin resistance fold]]
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| - | [[Category: Peptide binding protein]]
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| - | [[Category: Protein binding]]
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| - | [[Category: Solvent-exposed trp residue]]
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| - | [[Category: Thiocoraline]]
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| Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX, a protein with an unidentified function, is encoded by a gene of the thiocoraline biosynthetic gene cluster. The crystal structure of the full-length TioX protein at 2.15 A resolution reveals that TioX protomer shares an ancient betaalphabetabetabeta fold motif with glyoxalase I and bleomycin resistance protein families, despite a very low sequence homology. Intriguingly, four TioX monomers form a unique 2-fold symmetric tetrameric assembly that is stabilized by four intermolecular disulfide bonds formed cyclically between Cys60 and Cys66 of adjacent monomers. The arrangement of two of the four monomers in the TioX tetramer is analogous to that in dimeric bleomycin resistance proteins. This analogy indicates that this novel higher-order structural scaffold of TioX may have evolved to bind thiocoraline. Our equilibrium titration studies demonstrate the binding of a thiocoraline chromophore analog, quinaldic acid, to TioX, thereby substantiating this model. Furthermore, a strain of Streptomyces albus containing an exogenous thiocoraline gene cluster devoid of functional tioX maintains thiocoraline production, albeit with a lower yield. Taken together, these observations rule out a direct enzymatic function of TioX and suggest that TioX is involved in thiocoraline resistance or secretion.
A new scaffold of an old protein fold ensures binding to the bisintercalator thiocoraline.,Biswas T, Zolova OE, Lombo F, de la Calle F, Salas JA, Tsodikov OV, Garneau-Tsodikova S J Mol Biol. 2010 Mar 26;397(2):495-507. Epub 2010 Feb 1. PMID:20122935[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Biswas T, Zolova OE, Lombo F, de la Calle F, Salas JA, Tsodikov OV, Garneau-Tsodikova S. A new scaffold of an old protein fold ensures binding to the bisintercalator thiocoraline. J Mol Biol. 2010 Mar 26;397(2):495-507. Epub 2010 Feb 1. PMID:20122935 doi:10.1016/j.jmb.2010.01.053
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